Torpedo californica acetylcholinesterase complexed with Mg+2. Determined by X-ray diffraction at 1.85 Å resolution. Released 17 Mar 2021.
Explore 7B38 in 3D Show helices and sheets RCSB PDB PDBe
7B38 contains 37 α-helices and 27 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-10 | 4 | 1 |
| β-strand | 13-16 | 4 | 1 |
| β-strand | 18-22 | 5 | 2 |
| β-strand | 25-30 | 6 | 2 |
| β-strand | 31 | 1 | 3 |
| β-strand | 32-34 | 3 | 2 |
| β-strand | 36 | 1 | 4 |
| α-helix | 41-43 | 3 | |
| α-helix | 47-48 | 2 | |
| β-strand | 50 | 1 | 4 |
| α-helix | 51-53 | 3 | |
| β-strand | 57-59 | 3 | 1 |
| β-strand | 61 | 1 | 3 |
| α-helix | 65 | 1 | |
| β-strand | 66 | 1 | 5 |
| α-helix | 67-68 | 2 | |
| α-helix | 79-82 | 4 | |
| β-strand | 90 | 1 | 5 |
| β-strand | 96-101 | 6 | 2 |
| α-helix | 105-106 | 2 | |
| β-strand | 109-115 | 7 | 2 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-139 | 7 | |
| β-strand | 142-145 | 4 | 2 |
| α-helix | 152-155 | 4 | |
| β-strand | 157 | 1 | 6 |
| β-strand | 165 | 1 | 6 |
| α-helix | 168-183 | 16 | |
| α-helix | 184-187 | 4 | |
| β-strand | 189-199 | 11 | 2 |
| α-helix | 201-211 | 11 | |
| α-helix | 213-216 | 4 | |
| β-strand | 221-225 | 5 | 2 |
| β-strand | 236 | 1 | 7 |
| α-helix | 238-251 | 14 | |
| α-helix | 259-268 | 10 | |
| α-helix | 271-277 | 7 | |
| α-helix | 278-281 | 4 | |
| β-strand | 295 | 1 | 7 |
| α-helix | 305-311 | 7 | |
| β-strand | 318-324 | 7 | 2 |
| β-strand | 326 | 1 | 8 |
| α-helix | 329-335 | 7 | |
| α-helix | 349-359 | 11 | |
| α-helix | 365-375 | 11 | |
| α-helix | 384-396 | 13 | |
| α-helix | 397-401 | 5 | |
| α-helix | 402-412 | 11 | |
| β-strand | 417-423 | 7 | 2 |
| α-helix | 425-427 | 3 | |
| α-helix | 434-436 | 3 | |
| β-strand | 439 | 1 | 8 |
| α-helix | 444-447 | 4 | |
| α-helix | 450-452 | 3 | |
| α-helix | 454-456 | 3 | |
| α-helix | 460-479 | 20 | |
| α-helix | 490-491 | 2 | |
| α-helix | 493-495 | 3 | |
| β-strand | 501-505 | 5 | 2 |
| α-helix | 509-510 | 2 | |
| β-strand | 512-514 | 3 | 2 |
| α-helix | 518-522 | 5 | |
| α-helix | 523-527 | 5 | |
| α-helix | 528-534 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Acetylcholinesterase | A | protein | 532 | Tetronarce californica | P04058 (AlphaFold model) |
>7B38_1 Acetylcholinesterase (chains A) SELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTY PNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSG SSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWVHDN IQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRR RAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPT SLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHA NDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYLYFF NHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPN EPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNAT
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 4 |
| ZN | Zinc ion | Zn | 1 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Water and common crystallization additives (PGE, GOL, EDO, PEG) are not listed.
Torpedo californica acetylcholinesterase is stabilized by binding of a divalent metal ion to a novel and versatile 4D motif. Silman, I., Shnyrov, V.L., Ashani, Y. et al. Protein Sci (2021) 30:966-981. DOI 10.1002/pro.4061 · PubMed
Other PDB entries of the same protein (UniProt P04058 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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